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Structural and Functional Characterization of Pseudomonas aeruginosa CupB Chaperones

Pseudomonas aeruginosa, an important human pathogen, is estimated to be responsible for ∼10% of nosocomial infections worldwide. The pathogenesis of P. aeruginosa starts from its colonization in the damaged tissue or medical devices (e.g. catheters, prothesis and implanted heart valve etc.) facilita...

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Autores principales: Cai, Xun, Wang, Rui, Filloux, Alain, Waksman, Gabriel, Meng, Guoyu
Formato: Texto
Lenguaje:English
Publicado: Public Library of Science 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3031594/
https://www.ncbi.nlm.nih.gov/pubmed/21304995
http://dx.doi.org/10.1371/journal.pone.0016583
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author Cai, Xun
Wang, Rui
Filloux, Alain
Waksman, Gabriel
Meng, Guoyu
author_facet Cai, Xun
Wang, Rui
Filloux, Alain
Waksman, Gabriel
Meng, Guoyu
author_sort Cai, Xun
collection PubMed
description Pseudomonas aeruginosa, an important human pathogen, is estimated to be responsible for ∼10% of nosocomial infections worldwide. The pathogenesis of P. aeruginosa starts from its colonization in the damaged tissue or medical devices (e.g. catheters, prothesis and implanted heart valve etc.) facilitated by several extracellular adhesive factors including fimbrial pili. Several clusters containing fimbrial genes have been previously identified on the P. aeruginosa chromosome and named cup [1]. The assembly of the CupB pili is thought to be coordinated by two chaperones, CupB2 and CupB4. However, due to the lack of structural and biochemical data, their chaperone activities remain speculative. In this study, we report the 2.5 Å crystal structure of P. aeruginosa CupB2. Based on the structure, we further tested the binding specificity of CupB2 and CupB4 towards CupB1 (the presumed major pilus subunit) and CupB6 (the putative adhesin) using limited trypsin digestion and strep-tactin pull-down assay. The structural and biochemical data suggest that CupB2 and CupB4 might play different, but not redundant, roles in CupB secretion. CupB2 is likely to be the chaperone of CupB1, and CupB4 could be the chaperone of CupB4:CupB5:CupB6, in which the interaction of CupB4 and CupB6 might be mediated via CupB5.
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spelling pubmed-30315942011-02-08 Structural and Functional Characterization of Pseudomonas aeruginosa CupB Chaperones Cai, Xun Wang, Rui Filloux, Alain Waksman, Gabriel Meng, Guoyu PLoS One Research Article Pseudomonas aeruginosa, an important human pathogen, is estimated to be responsible for ∼10% of nosocomial infections worldwide. The pathogenesis of P. aeruginosa starts from its colonization in the damaged tissue or medical devices (e.g. catheters, prothesis and implanted heart valve etc.) facilitated by several extracellular adhesive factors including fimbrial pili. Several clusters containing fimbrial genes have been previously identified on the P. aeruginosa chromosome and named cup [1]. The assembly of the CupB pili is thought to be coordinated by two chaperones, CupB2 and CupB4. However, due to the lack of structural and biochemical data, their chaperone activities remain speculative. In this study, we report the 2.5 Å crystal structure of P. aeruginosa CupB2. Based on the structure, we further tested the binding specificity of CupB2 and CupB4 towards CupB1 (the presumed major pilus subunit) and CupB6 (the putative adhesin) using limited trypsin digestion and strep-tactin pull-down assay. The structural and biochemical data suggest that CupB2 and CupB4 might play different, but not redundant, roles in CupB secretion. CupB2 is likely to be the chaperone of CupB1, and CupB4 could be the chaperone of CupB4:CupB5:CupB6, in which the interaction of CupB4 and CupB6 might be mediated via CupB5. Public Library of Science 2011-01-31 /pmc/articles/PMC3031594/ /pubmed/21304995 http://dx.doi.org/10.1371/journal.pone.0016583 Text en Cai et al. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Cai, Xun
Wang, Rui
Filloux, Alain
Waksman, Gabriel
Meng, Guoyu
Structural and Functional Characterization of Pseudomonas aeruginosa CupB Chaperones
title Structural and Functional Characterization of Pseudomonas aeruginosa CupB Chaperones
title_full Structural and Functional Characterization of Pseudomonas aeruginosa CupB Chaperones
title_fullStr Structural and Functional Characterization of Pseudomonas aeruginosa CupB Chaperones
title_full_unstemmed Structural and Functional Characterization of Pseudomonas aeruginosa CupB Chaperones
title_short Structural and Functional Characterization of Pseudomonas aeruginosa CupB Chaperones
title_sort structural and functional characterization of pseudomonas aeruginosa cupb chaperones
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3031594/
https://www.ncbi.nlm.nih.gov/pubmed/21304995
http://dx.doi.org/10.1371/journal.pone.0016583
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